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O42227 (HDA1B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable histone deacetylase 1-B
Short name=HD1-B
EC=3.5.1.98
Alternative name(s):
RPD3 homolog
Gene names
Name:hdac1-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Ref.3

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

Found in a large complex with RBBP4 and MI-2. Ref.2

Subcellular location

Cytoplasm. Nucleus Ref.3.

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Probable histone deacetylase 1-B
PRO_0000114692

Regions

Region10 – 321312Histone deacetylase
Compositional bias299 – 3024Poly-Gly

Sites

Active site1411 By similarity

Experimental info

Mutagenesis1411H → A: Abolishes histone deacetylase activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O42227 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: CA92DE34D36E39E8

FASTA48054,893
        10         20         30         40         50         60 
MALSQGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAS 

        70         80         90        100        110        120 
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS 

       130        140        150        160        170        180 
AVKLNKQQTD ISVNWSGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV VYIDIDIHHG 

       190        200        210        220        230        240 
DGVEEAFYTT DRVMSVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 

       250        260        270        280        290        300 
FKPVMTKVME MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPMLMLGG 

       310        320        330        340        350        360 
GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 

       370        380        390        400        410        420 
KIKQRLFENL RMLPHAPGVQ MQAIPEDSVH DDSGEEDEED PDKRISIRSS DKRIACDEEF 

       430        440        450        460        470        480 
SDSEDEGEGG RKNVANFKKV KRVKTEEEKE GEDKKDVKEE EKAKDEKTDS KRVKEETKSV

« Hide

References

[1]"Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase."
Wong J., Patterton D., Imhof A., Guschin D., Shi Y.-B., Wolffe A.P.
EMBO J. 17:520-534(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase."
Wade P.A., Jones P.L., Vermaak D., Wolffe A.P.
Curr. Biol. 8:843-846(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RBBP4 AND MI-2.
[3]"Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte."
Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P.
Mol. Cell. Biol. 19:5847-5860(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP4, MUTAGENESIS OF HIS-141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF020658 mRNA. Translation: AAC60346.1.
UniGeneXl.20805.

3D structure databases

ProteinModelPortalO42227.
ModBaseSearch...

Proteomic databases

PRIDEO42227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-865283. hdac1.

Phylogenomic databases

HOVERGENHBG057112.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Entry information

Entry nameHDA1B_XENLA
AccessionPrimary (citable) accession number: O42227
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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